CAD89_DROME
ID CAD89_DROME Reviewed; 2240 AA.
AC Q9VEU1; Q6NR53; Q9GR86;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cadherin-89D;
DE Flags: Precursor;
GN Name=Cad89D; ORFNames=CG14900;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hirano S., Kimura H., Takeichi M., Uemura T.;
RT "A novel member of the Drosophila cadherin superfamily, Cad89D.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC preferentially interact with themselves in a homophilic manner in
CC connecting cells (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain. {ECO:0000250}.
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DR EMBL; AB053260; BAB20634.1; -; mRNA.
DR EMBL; AE014297; AAF55327.3; -; Genomic_DNA.
DR EMBL; BT010226; AAQ23544.1; -; mRNA.
DR RefSeq; NP_650554.3; NM_142297.4.
DR AlphaFoldDB; Q9VEU1; -.
DR BioGRID; 67051; 3.
DR DIP; DIP-18418N; -.
DR IntAct; Q9VEU1; 5.
DR STRING; 7227.FBpp0290916; -.
DR GlyGen; Q9VEU1; 19 sites.
DR PaxDb; Q9VEU1; -.
DR PRIDE; Q9VEU1; -.
DR EnsemblMetazoa; FBtr0301702; FBpp0290916; FBgn0038439.
DR GeneID; 42006; -.
DR KEGG; dme:Dmel_CG14900; -.
DR UCSC; CG14900-RA; d. melanogaster.
DR CTD; 42006; -.
DR FlyBase; FBgn0038439; Cad89D.
DR VEuPathDB; VectorBase:FBgn0038439; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000167267; -.
DR HOGENOM; CLU_001273_0_0_1; -.
DR InParanoid; Q9VEU1; -.
DR OMA; NCAVGTE; -.
DR OrthoDB; 13033at2759; -.
DR SignaLink; Q9VEU1; -.
DR BioGRID-ORCS; 42006; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42006; -.
DR PRO; PR:Q9VEU1; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038439; Expressed in insect adult head and 4 other tissues.
DR Genevisible; Q9VEU1; DM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; ISM:FlyBase.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:FlyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISM:FlyBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR Pfam; PF00028; Cadherin; 6.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 12.
DR SUPFAM; SSF49313; SSF49313; 11.
DR PROSITE; PS00232; CADHERIN_1; 7.
DR PROSITE; PS50268; CADHERIN_2; 12.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..2240
FT /note="Cadherin-89D"
FT /id="PRO_0000004008"
FT TOPO_DOM ?..1883
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1884..1904
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1905..2240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 70..179
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 180..295
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 296..411
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 412..528
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 529..643
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 824..927
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 928..1087
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1171..1284
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1285..1389
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1411..1520
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1534..1660
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1661..1774
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 814..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1930..1972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2121..2140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1951..1972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 822
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 833
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 983
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 989
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1006
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 8
FT /note="M -> R (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="D -> E (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="N -> Y (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="M -> I (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="T -> S (in Ref. 4; AAQ23544)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="A -> G (in Ref. 4; AAQ23544)"
FT /evidence="ECO:0000305"
FT CONFLICT 702
FT /note="E -> D (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 823
FT /note="I -> L (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 945
FT /note="E -> G (in Ref. 4; AAQ23544)"
FT /evidence="ECO:0000305"
FT CONFLICT 997
FT /note="S -> P (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 1187
FT /note="T -> A (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 1258
FT /note="V -> G (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 1319
FT /note="I -> M (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 1330
FT /note="F -> S (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 1342
FT /note="G -> S (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 1497
FT /note="P -> A (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 1504
FT /note="I -> V (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 1606
FT /note="S -> C (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 1618
FT /note="S -> N (in Ref. 4; AAQ23544)"
FT /evidence="ECO:0000305"
FT CONFLICT 1633
FT /note="D -> G (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 1660
FT /note="F -> Y (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 1745
FT /note="D -> V (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 1801
FT /note="P -> R (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 1892
FT /note="L -> R (in Ref. 1; BAB20634)"
FT /evidence="ECO:0000305"
FT CONFLICT 2095
FT /note="T -> A (in Ref. 4; AAQ23544)"
FT /evidence="ECO:0000305"
FT CONFLICT 2138
FT /note="D -> G (in Ref. 4; AAQ23544)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2240 AA; 250636 MW; 7D8001742A8AD826 CRC64;
MDSEAYPMKS SVKISQKKKA SQDMAVICVW VMPLAVFGLI AIGQAAKTGQ VQASSGSCAF
HTLDGVAAES EGVRFIRLRE DAQVGKEILR LQAYPRSTAA LKGADASGDH KYFNLTEHNA
TTLVVSLARS LERLVDRDVP RNLLKFRILC AGKQEKLEEG SYLSITVYIE DVNDNAPEFL
NVPYVVDVDE NTSIESIIFE GVQAFDRDKP NTPNSEVHFS MSTVPEQLSA DGSPYFALKS
PHRPLLILKR ELDFDNGIRQ FKLPIFAWDR GTPANQANTT ITINVRDVDD LPPKFTEGVY
RTRINEFYPM TGVPIRIPLY FAPPIMAFDQ DSLNASLVYD IISGNERQLF RVNPHNGVMY
LQKEIDLEEE SLPGNTFVLQ LEARQKDNPL KKALARIEVE VLDLNDNVPE FEADYYNISI
VENLPTGFSV LQVNAVDRDQ GENSEFLYNL VETKDAAGAF RIDSRTGWIT VRDDRLLDRE
QRRSIQLNVE ALERNPSYLD DKHLKKPGPS KVQVEITLLD TNDNTPKFEH GNLYEFKVPI
NAPTGYVIGQ VVAHDPDEGP NGHLLYELQR PKGSGYIPFR LDNKNGTIYV GGPLRRGRIA
VFVEATDQPT NPSERRFSLA VITIEVYATI DDQAIDFVGA PYEFWVGANT PLGTSVGQVR
TTLIYEGGDE IMYDLLHTYS EGVPFAIEER SGIITVIREL SEFKRKVYQF EAVANYLFAN
SSQSLVMSRS SSPLTTIASP AELSDEGVLI TNLTIHIVNK PEQKVPLRPV IEEINMNVIH
FHVEENVVGG IIGQLLYKNG INLVNNELGT YREMPSEPTS RNITMGSRFR SRNRSRSSKS
KRRLPRRLVG DANIKLRYII ANQQEVVNKI SITEDGTLLT LTGLDREQQP SYELTVIVEY
STGLVSGAGI YQVNIKVDDV NDNAPKFNAL TYVGLINENC VVGTELSMNH AILIQDADEG
PNAEFRVQLQ GDYSDEFSIE YVNGTSSENS THHKMPSTTG AFNIFNLTDQ WNDEFKYQEL
HTTFMQTNFK LSSGPYFRIS YTGKRGLDRE KQQLYNLKII AADTGGLSGY AHLTVLVADV
NDNAPMFERI SVFKDSRLEI REYTTDMEIY FVESSSGMTA PQATAAMMLA PPPYHIPGSP
RFNVDRERSV GAGLGVVARA KSRRRMVRAL TTKCPLFAIY EDTPVGTKVL QLSASDEDFG
KNALLHYELQ GEQVERTPGM PMLRVHGVKY FAIDKLSGEL SVNYPLSANI EIMLNLTVTD
IDGLKDSTCL RFTVMDVNNH APTFKKSWYS FDTPEGEYKD SVLGQLTAID MDFGENANIT
YTLSDSHLPF TIKPASGVLK IGGQLDRELK DKYSFQVIAT DNAPVMQRMS SSVDVEVNVL
DINDNRPEFI GYDDQTKAVK FIPSVADRTL MLPVYKAYLD RSTQPGTFVR QLTAIDKDNV
GNGNGLVLYS IRHQEMQAPL FQIDSRDGTI STISRINGYN DYEHLNVSVI ASDVGSPALS
ATAIVIVNLQ GQAVTDPPKS TPKPEPPANV TVFQHAYYEV KLTENNEAPI EVMRLNLSAG
LNPENYRWSL WLEEGLDETD AHPPFEYDAK NMLLYALKPF DREHISRYQL RIRADRLSRE
ARNYARVSYP VVDERIEGLS LNECRILVHI ADENDNAPKF RGNGQPIVAV LPQSASFGYP
VTRVEANDLD EGLNAEIRYR LLNEPARLFG IDELSGNIRL LGELSRTEHI YGFDVKATDR
MGADDGRSGI VNVFVYIINE AKQVRLVVAG MPVEVERRIE GLMEALSDAI GKDVRVRLLE
PYSGGLEPAT NAYIYAVDPH TNSIMEMEQL QDALAGLQLD ALQLQQQKLD GGKPMPRILE
LAEFGQLARP AHASASSFMG GLEFVTVVLL ALISLGALIA ACCYVCMRQK RRLWSQRDFS
ASDAGLTYTI AGIGSPRGQK QRRQRQQRHT QRCSKGSTGS QRPTSAFMPE SVCSSAQTQS
TATATEKLEQ QLHHHHQQQA MATQQQHHQY LNEQQRQQKR EYIDVPLPKS IAKAAAVTSG
GDGAVGVGST PFVLKYNACQ PVNNLNNYET SLFSLHSTGQ DSGVEFLSSR ELYETSPDSF
QHGGSKRGNN TEVLCPRHAK AHLELRQPNT DSSDTYEDSL KTDEPLVAHN CRSANCEHRQ
HQQHPSHHPH YQNTRFEKRS CVRHSFSGVK DDLMQQSPQI SLRPRGHALR NSMNDLEQRL
HNLEQSFRRP LEFSKSNSLF
